Search Results
Overview
| Uniprot ID | Q9UKL0 |
|---|---|
| Protein Name | REST corepressor 1 |
| Gene Name | RCOR1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 14 | KGPEVSGKRRGRNNA |
| 242 | SWKKTRTKTSVMDRH |
| 285 | DQNKESKKEVPPTET |
| 297 | TETVPQVKKEKHSTQ |
| 298 | ETVPQVKKEKHSTQA |
| 349 | DMELVSVKRQIQNIK |
| 356 | KRQIQNIKQTNSALK |
| 365 | TNSALKEKLDGGIEP |
| 381 | RLPEVIQKCNARWTT |
| 459 | PSNQKPVKSPDNSIK |
| 466 | KSPDNSIKMPEEEDE |
| 7 | *MPAMVEKGPEVSGK |
Function
Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:1990391 | DNA repair complex |
| Cellular Component | GO:0000118 | histone deacetylase complex |
| Cellular Component | GO:0035097 | histone methyltransferase complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005667 | transcription regulator complex |
| Cellular Component | GO:0017053 | transcription repressor complex |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0003714 | transcription corepressor activity |
| Biological Process | GO:0006325 | chromatin organization |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0030218 | erythrocyte differentiation |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0010629 | negative regulation of gene expression |
| Biological Process | GO:0045654 | positive regulation of megakaryocyte differentiation |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.